2f48

Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi

spinqualitylabelsall models 2f48, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f48 is a 2 chain structure with sequence from Borreliella burgdorferi B31. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.11Å Ligands: AF3, FBP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PFP_BORBU Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01980] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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